HSP98_NEUCR
ID HSP98_NEUCR Reviewed; 927 AA.
AC P31540; Q7RYM4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Heat shock protein hsp98;
DE AltName: Full=Protein aggregation-remodeling factor hsp98;
GN Name=hsp98; ORFNames=NCU00104;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP PROTEIN SEQUENCE OF 312-340.
RC STRAIN=74A;
RX PubMed=1472534; DOI=10.1016/0304-4165(92)90087-b;
RA Vassilev A.O., Plesofsky-Vig N., Brambl R.;
RT "Isolation, partial amino acid sequence, and cellular distribution of heat-
RT shock protein hsp98 from Neurospora crassa.";
RL Biochim. Biophys. Acta 1156:1-6(1992).
CC -!- FUNCTION: Required, in concert with Hsp40 and Hsp70 and small Hsps, for
CC the dissociation, resolubilization and refolding of aggregates of
CC damaged proteins after heat or other environmental stresses. Extracts
CC proteins from aggregates by unfolding and threading them in an ATP-
CC dependent process through the axial channel of the protein hexamer,
CC after which they can be refolded by components of the Hsp70/Hsp40
CC chaperone system (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer, forming a ring with a central pore.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Note=More
CC concentrated in polyribosomes than in monoribosomes, and preferentially
CC localized in the large subunit.
CC -!- DOMAIN: Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per
CC monomer. ATP binding to NBD1 triggers binding of polypeptides and
CC stimulates ATP hydrolysis at NBD2. Nucleotide binding to NBD2 is
CC crucial for oligomerization (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The C-terminal extension is involved in oligomerization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; CM002238; EAA27992.1; -; Genomic_DNA.
DR PIR; S28174; S28174.
DR RefSeq; XP_957228.1; XM_952135.3.
DR AlphaFoldDB; P31540; -.
DR SMR; P31540; -.
DR STRING; 5141.EFNCRP00000000125; -.
DR PRIDE; P31540; -.
DR EnsemblFungi; EAA27992; EAA27992; NCU00104.
DR GeneID; 3873391; -.
DR KEGG; ncr:NCU00104; -.
DR VEuPathDB; FungiDB:NCU00104; -.
DR HOGENOM; CLU_005070_4_2_1; -.
DR InParanoid; P31540; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0140602; C:nucleolar ring; IEA:EnsemblFungi.
DR GO; GO:0140453; C:protein aggregate center; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0070370; P:cellular heat acclimation; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0071218; P:cellular response to misfolded protein; IEA:EnsemblFungi.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0043335; P:protein unfolding; IBA:GO_Central.
DR Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; Stress response.
FT CHAIN 1..927
FT /note="Heat shock protein hsp98"
FT /id="PRO_0000191213"
FT DOMAIN 2..162
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 7..87
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 99..162
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 179..428
FT /note="NBD1"
FT REGION 454..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..752
FT /note="NBD2"
FT REGION 908..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 429..553
FT /evidence="ECO:0000255"
FT BINDING 224..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 635..642
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 927 AA; 103182 MW; 46F263181BBD9D18 CRC64;
MTSKMEFTDR AKKALEDAMA LAEQYAHSQL LPVHLAVALL DPLPDPSKDQ QNAPAGATSS
LFRQVIERAH GDPQLFDRAL KKALVRLPSQ DPPPDHVSMA PSFHTVLRKA NELQKTQKDT
YIAVDHLITA LAEEPSIMNA LKEANIPKPK LVTDAIQAIR GTKRVDSRNA DTEEEHENLA
KFTIDMTAMA REGKIDPVIG REEEIRRVIR ILSRRTKNNP VLIGEPGVGK TTVVEGLAQR
IVNADVPDNL ANCKLLSLDV GALVAGSKYR GEFEERMKGV LKEISESKEM IILFIDEIHL
LMGAGASGEG GMDAANLLKP MLARGQLHCI GATTLAEYRK YIEKDAAFER RFQQVIVKEP
SVSETISILR GLKEKYEVHH GVTISDAAIV AAANLAARYL TSRRLPDSAI DLIDEAAAAV
RVARESQPEI IDSLERKLRQ LKIEIHALSR EKDEASKARL EQAKKDAENV EEELRPLREK
YEQEKQRAKA LQEARMKLES LRQKAEEASR MGDHSRAADL QYYAIPEQEA VIKRLEKEKA
AADAALNAAA AETGGAMITD VVGPDQINEI VARWTGIPVT RLKTSEKEKL LHMEKHLSKI
VVGQKEAVQS VSNAIRLQRS GLSNPNQPPS FLFCGPSGTG KTLLTKALAE FLFDDPKAMI
RFDMSEYQER HSLSRMIGAP PGYVGHDSGG QLTEALRRKP FSILLFDEVE KAAKEVLTVL
LQLMDDGRIT DGQGRVVDAR NCIVVMTSNL GAEYLSRPNA KDGKIDPTTR ELVMNALRNY
FLPEFLNRIS SIVIFNRLTR REIRKIVELR IAEIQKRLQD NDRNVKIEVS EEAKDKLGAL
GYSPAYGARP LQRVLEKEVL NRLAVLILRG SIRDGEVARV VVQDGKITVL PNHPEVNDED
DEMMLDEEDA VDEVAPESEM DEDLYDD
